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Zinc in PDB 2ar3: E90A Mutant Structure of Plyl

Enzymatic activity of E90A Mutant Structure of Plyl

All present enzymatic activity of E90A Mutant Structure of Plyl:
3.5.1.28;

Protein crystallography data

The structure of E90A Mutant Structure of Plyl, PDB code: 2ar3 was solved by L.Y.Low, C.Yang, M.Perego, A.Osterman, R.C.Liddington, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.83 / 2.20
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 163.644, 163.644, 38.462, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the E90A Mutant Structure of Plyl (pdb code 2ar3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the E90A Mutant Structure of Plyl, PDB code: 2ar3:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2ar3

Go back to Zinc Binding Sites List in 2ar3
Zinc binding site 1 out of 3 in the E90A Mutant Structure of Plyl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E90A Mutant Structure of Plyl within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn161

b:38.5
occ:1.00
ND1 A:HIS29 2.2 32.2 1.0
ND1 A:HIS129 2.3 30.0 1.0
SG A:CYS137 2.4 36.0 1.0
O4 A:PO4162 2.4 61.7 1.0
O2 A:PO4162 2.8 62.5 1.0
P A:PO4162 3.0 62.6 1.0
CG A:HIS29 3.1 33.2 1.0
CG A:HIS129 3.2 31.3 1.0
CB A:CYS137 3.2 32.2 1.0
CB A:HIS29 3.2 32.8 1.0
CE1 A:HIS29 3.3 32.0 1.0
CB A:HIS129 3.3 31.3 1.0
O3 A:PO4162 3.4 62.2 1.0
CE1 A:HIS129 3.4 30.8 1.0
CA A:HIS29 4.0 33.7 1.0
CD2 A:HIS29 4.3 32.4 1.0
O A:ALA74 4.3 43.5 1.0
NE2 A:HIS29 4.3 33.9 1.0
O A:HOH191 4.3 51.4 1.0
CD2 A:HIS129 4.4 31.2 1.0
O1 A:PO4162 4.4 62.6 1.0
NE2 A:HIS129 4.4 30.4 1.0
O A:ASN30 4.5 37.4 1.0
N A:ASN30 4.6 34.7 1.0
CA A:CYS137 4.6 35.2 1.0
CA A:HIS129 4.8 33.5 1.0
O A:HOH163 4.9 27.3 1.0
C A:HIS29 4.9 35.1 1.0
C A:CYS137 5.0 36.3 1.0

Zinc binding site 2 out of 3 in 2ar3

Go back to Zinc Binding Sites List in 2ar3
Zinc binding site 2 out of 3 in the E90A Mutant Structure of Plyl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E90A Mutant Structure of Plyl within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn161

b:38.9
occ:1.00
ND1 B:HIS129 2.2 29.8 1.0
O4 B:PO4162 2.2 51.9 1.0
ND1 B:HIS29 2.3 30.9 1.0
SG B:CYS137 2.4 36.9 1.0
O2 B:PO4162 2.9 52.8 1.0
CG B:HIS129 3.1 31.4 1.0
P B:PO4162 3.1 57.0 1.0
CG B:HIS29 3.2 35.4 1.0
CE1 B:HIS129 3.2 30.7 1.0
CB B:HIS129 3.3 30.1 1.0
CE1 B:HIS29 3.3 34.2 1.0
CB B:CYS137 3.3 33.7 1.0
CB B:HIS29 3.4 34.1 1.0
O B:HOH218 4.0 54.4 1.0
O1 B:PO4162 4.1 54.1 1.0
CA B:HIS29 4.1 34.1 1.0
O3 B:PO4162 4.2 56.6 1.0
O B:HOH222 4.2 60.6 1.0
CD2 B:HIS129 4.2 31.9 1.0
NE2 B:HIS129 4.3 32.8 1.0
O B:ALA74 4.3 38.4 1.0
CD2 B:HIS29 4.4 35.5 1.0
NE2 B:HIS29 4.4 36.0 1.0
O B:ASN30 4.6 35.8 1.0
CA B:CYS137 4.7 34.1 1.0
N B:ASN30 4.7 36.7 1.0
CA B:HIS129 4.8 31.3 1.0
O B:HOH168 4.9 29.7 1.0
C B:HIS29 5.0 35.8 1.0

Zinc binding site 3 out of 3 in 2ar3

Go back to Zinc Binding Sites List in 2ar3
Zinc binding site 3 out of 3 in the E90A Mutant Structure of Plyl


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of E90A Mutant Structure of Plyl within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn161

b:40.2
occ:1.00
ND1 C:HIS129 2.2 36.4 1.0
SG C:CYS137 2.3 38.3 1.0
O3 C:PO4163 2.3 73.0 1.0
ND1 C:HIS29 2.4 44.0 1.0
O1 C:PO4163 2.6 73.4 1.0
P C:PO4163 2.8 74.9 1.0
CG C:HIS129 3.1 38.3 1.0
CE1 C:HIS129 3.2 39.1 1.0
CG C:HIS29 3.2 44.4 1.0
CB C:HIS129 3.3 40.4 1.0
CB C:CYS137 3.3 41.0 1.0
O4 C:PO4163 3.3 75.2 1.0
CB C:HIS29 3.4 41.5 1.0
CE1 C:HIS29 3.5 44.3 1.0
CA C:HIS29 4.0 44.2 1.0
O C:ALA74 4.2 56.0 1.0
O2 C:PO4163 4.2 73.5 1.0
CD2 C:HIS129 4.2 38.0 1.0
NE2 C:HIS129 4.3 38.7 1.0
CD2 C:HIS29 4.5 45.3 1.0
NE2 C:HIS29 4.5 44.2 1.0
N C:ASN30 4.6 46.6 1.0
CA C:CYS137 4.7 42.3 1.0
CA C:HIS129 4.8 39.0 1.0
O C:HOH164 4.8 31.9 1.0
C C:HIS29 4.9 45.5 1.0
O C:ASN30 4.9 50.0 1.0

Reference:

L.Y.Low, C.Yang, M.Perego, A.Osterman, R.C.Liddington. Structure and Lytic Activity of A Bacillus Anthracis Prophage Endolysin. J.Biol.Chem. V. 280 35433 2005.
ISSN: ISSN 0021-9258
PubMed: 16103125
DOI: 10.1074/JBC.M502723200
Page generated: Wed Dec 16 03:17:52 2020

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